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Characterization and potential application of an α-amylase (BmAmy1) selected during silkworm domestication.
Yan, Hao; Liu, Qingsong; Wen, Feng; Bai, Bingchuan; Wen, Yuchan; Chen, Wenwen; Lu, Wei; Lin, Ying; Xia, Qingyou; Wang, Genhong.
Affiliation
  • Yan H; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Liu Q; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Wen F; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Bai B; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Wen Y; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Chen W; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Lu W; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Lin Y; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Xia Q; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
  • Wang G; State Key Laboratory of Silkworm Genome Biology, Biological Science Research Center, Southwest University, Chongqing 400716, China; Chongqing Key Laboratory of Sericultural Science, Southwest University, Chongqing 400716, China; Chongqing Engineering and Technology Research Center for Novel Silk Mat
Int J Biol Macromol ; 167: 1102-1112, 2021 Jan 15.
Article in En | MEDLINE | ID: mdl-33188814
Efficient resource utilization plays a central role in the high productivity of domesticated plants and animals. Whether artificial selection acts on digestive enzymes in the domesticated silkworm (Bombyx mori), which is larger than its wild ancestor, Bombyx mandarina (B. mandarina), remains unknown. In this study, we present the characteristics of a novel alpha-amylase, BmAmy1, in B. mori. The activity of recombinant BmAmy1 was maximal at 35 °C and pH 9.0, and could be suppressed by amylase inhibitors from mulberry, the exclusive food source of silkworms. Three different transposable element fragments, which were independently inserted in the 5'-upstream regulatory region, might be responsible for the enhanced expression of BmAmy1 in different domesticated silkworm strains as revealed by dual-luciferase reporter assay. The BmAmy1 overexpression increased the weight of female and male B. mori by 11.9% and 6.8%, respectively, compared with non-transgenic controls. Our results emphasize that, by exploring the genetic mechanisms of human-selected traits, the domestication process could be further accelerated through genetic engineering and targeted breeding.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Selection, Genetic / Bombyx / Alpha-Amylases / Domestication Limits: Animals Language: En Journal: Int J Biol Macromol Year: 2021 Document type: Article Country of publication: Netherlands

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Selection, Genetic / Bombyx / Alpha-Amylases / Domestication Limits: Animals Language: En Journal: Int J Biol Macromol Year: 2021 Document type: Article Country of publication: Netherlands